Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E

• Kubota, Hiroaki

  Department of Physics, Faculty of Science and Engineering, Waseda University; Department of Microbiology, Tokyo Metropolitan Institute of Public Health

• Ogawa, Hiroyuki

  Department of Physics, Faculty of Science and Engineering, Waseda University

• Miyazaki, Makito

  Hakubi Center for Advanced Research, Kyoto University; Department of Physics, Graduate School of Science, Kyoto University; PRESTO, Japan Science and Technology Agency; Institut Curie, PSL Research University, CNRS

• Ishii, Shuya

  Department of Physics, Faculty of Science and Engineering, Waseda University; Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology

• Oyama, Kotaro

  Department of Physics, Faculty of Science and Engineering, Waseda University; PRESTO, Japan Science and Technology Agency; Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology

• Kawamura, Yuki

  Department of Physics, Faculty of Science and Engineering, Waseda University

• Ishiwata, Shin’ichi

  Department of Physics, Faculty of Science and Engineering, Waseda University

• Suzuki, Madoka

  Institute for Protein Research, Osaka University

Abstract

Drebrin E is a regulatory protein of intracellular force produced by actomyosin complexes, that is, myosin molecular motors interacting with actin filaments. The expression level of drebrin E in nerve cells decreases as the animal grows, suggesting its pivotal but unclarified role in neuronal development. Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. The direct observation of quantum dot-labeled drebrin E implies its stable binding to actin filaments during the heat-induced sliding. Our results suggest that drebrin E allosterically modifies the actin filament structure to regulate cooperatively the actomyosin activity at the maintained in vivo body temperature.

Journal

• Nano Letters

  Nano Letters 21 (22), 9526-9533, 2021-11-24

  American Chemical Society (ACS)

Keywords

• actin-binding protein
• cytoskeleton
• heat pulse
• molecular motor
• motility assay
• nanofilament regulation
• temperature imaging

Details

• CRID: 1050853179565363456
• NII Article ID: 120007171008
• DOI: 10.1021/acs.nanolett.1c02955
• ISSN: 15306992
• ISSN: 15306984
• HANDLE: 2433/266182
• Web Site: https://pubs.acs.org/doi/pdf/10.1021/acs.nanolett.1c02955
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • Crossref
  • CiNii Articles
  • KAKEN